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Protein

Ras-related GTP-binding protein A

Gene

Rraga

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates to the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death.By similarity

Enzyme regulationi

The activation of GTP-binding proteins is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). The GATOR1 complex functions as a GAP and stimulates RRAGA GTPase activity to turn it into its inactive GDP-bound form.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi62 – 665GTPBy similarity
Nucleotide bindingi127 – 1304GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related GTP-binding protein ACurated
Short name:
Rag ABy similarity
Short name:
RagABy similarity
Gene namesi
Name:RragaImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1915691. Rraga.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Lysosome By similarity

  • Note: Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Ras-related GTP-binding protein APRO_0000239946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki142 – 142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki220 – 220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki244 – 244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei309 – 3091PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated. 'Lys-68'-linked polyubiquitination of the GDP-bound inactive form of RRAGA at Lys-142, Lys-220, Lys-230 and Lys-244 by RNF152 is increased in response to amino acid starvation. Polyubiquitination promotes interaction with the GATOR1 complex. This does not affect RRAGA degradation.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ80X95.
MaxQBiQ80X95.
PaxDbiQ80X95.
PeptideAtlasiQ80X95.
PRIDEiQ80X95.

PTM databases

iPTMnetiQ80X95.
PhosphoSiteiQ80X95.

Expressioni

Gene expression databases

BgeeiENSMUSG00000070934.
CleanExiMM_RRAGA.
GenevisibleiQ80X95. MM.

Interactioni

Subunit structurei

Can occur as a homodimer or as a heterodimer with RRAGC or RRAGD in a sequence-independent manner; heterodimerization stabilizes proteins of the heterodimer. In complex with RRAGC, but not with RRAGB, interacts with RPTOR. The GTP-bound form of RRAGA interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGA and is negatively regulated by amino acids. The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor. Interacts (inactive GDP-bound form) with RNF152; stimulated by amino acid starvation. Interacts (polyubiquitinated) with the GATOR1 complex; inactivates RRAGA. Interacts (polyubiquitinated) with TSC2 (By similarity). Interacts with SESN1, SESN2 AND SESN3 (PubMed:25259925).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ80X95. 3 interactions.
STRINGi10090.ENSMUSP00000088591.

Structurei

3D structure databases

ProteinModelPortaliQ80X95.
SMRiQ80X95. Positions 7-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTR/RAG GTP-binding protein family.Curated

Phylogenomic databases

eggNOGiKOG3886. Eukaryota.
ENOG410XQ0R. LUCA.
GeneTreeiENSGT00550000074769.
HOGENOMiHOG000173258.
HOVERGENiHBG052715.
InParanoidiQ80X95.
KOiK16185.
OMAiVHYYQSC.
OrthoDBiEOG091G050Q.
PhylomeDBiQ80X95.
TreeFamiTF300616.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 1 hit.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q80X95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNTAMKKKV LLMGKSGSGK TSMRSIIFAN YIARDTRRLG ATIDVEHSHV
60 70 80 90 100
RFLGNLVLNL WDCGGQDTFM ENYFTSQRDN IFRNVEVLIY VFDVESRELE
110 120 130 140 150
KDMHYYQSCL EAILQNSPDA KIFCLVHKMD LVQEDQRDLI FKEREEDLRR
160 170 180 190 200
LSRPLECACF RTSIWDETLY KAWSSIVYQL IPNVQQLEMN LRNFAQIIEA
210 220 230 240 250
DEVLLFERAT FLVISHYQCK EQRDVHRFEK ISNIIKQFKL SCSKLAASFQ
260 270 280 290 300
SMEVRNSNFA AFIDIFTSNT YVMVVMSDPS IPSAATLINI RNARKHFEKL
310
ERVDGPKHSL LMR
Length:313
Mass (Da):36,566
Last modified:June 1, 2003 - v1
Checksum:iB0DA1FC8FA6B766A
GO

Sequence cautioni

The sequence AAH37615 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC25103 differs from that shown. Reason: Frameshift at positions 183 and 193. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004955 mRNA. Translation: BAC25103.1. Frameshift.
AK144591 mRNA. Translation: BAE25953.1.
AL824707 Genomic DNA. Translation: CAM27444.1.
BC037615 mRNA. Translation: AAH37615.1. Different initiation.
BC048245 mRNA. Translation: AAH48245.1.
CCDSiCCDS18306.1.
RefSeqiNP_848463.1. NM_178376.3.
UniGeneiMm.31178.

Genome annotation databases

EnsembliENSMUST00000091064; ENSMUSP00000088591; ENSMUSG00000070934.
GeneIDi68441.
KEGGimmu:68441.
UCSCiuc008tlw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004955 mRNA. Translation: BAC25103.1. Frameshift.
AK144591 mRNA. Translation: BAE25953.1.
AL824707 Genomic DNA. Translation: CAM27444.1.
BC037615 mRNA. Translation: AAH37615.1. Different initiation.
BC048245 mRNA. Translation: AAH48245.1.
CCDSiCCDS18306.1.
RefSeqiNP_848463.1. NM_178376.3.
UniGeneiMm.31178.

3D structure databases

ProteinModelPortaliQ80X95.
SMRiQ80X95. Positions 7-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80X95. 3 interactions.
STRINGi10090.ENSMUSP00000088591.

PTM databases

iPTMnetiQ80X95.
PhosphoSiteiQ80X95.

Proteomic databases

EPDiQ80X95.
MaxQBiQ80X95.
PaxDbiQ80X95.
PeptideAtlasiQ80X95.
PRIDEiQ80X95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091064; ENSMUSP00000088591; ENSMUSG00000070934.
GeneIDi68441.
KEGGimmu:68441.
UCSCiuc008tlw.2. mouse.

Organism-specific databases

CTDi10670.
MGIiMGI:1915691. Rraga.

Phylogenomic databases

eggNOGiKOG3886. Eukaryota.
ENOG410XQ0R. LUCA.
GeneTreeiENSGT00550000074769.
HOGENOMiHOG000173258.
HOVERGENiHBG052715.
InParanoidiQ80X95.
KOiK16185.
OMAiVHYYQSC.
OrthoDBiEOG091G050Q.
PhylomeDBiQ80X95.
TreeFamiTF300616.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiRraga. mouse.
PROiQ80X95.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000070934.
CleanExiMM_RRAGA.
GenevisibleiQ80X95. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 1 hit.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRRAGA_MOUSE
AccessioniPrimary (citable) accession number: Q80X95
Secondary accession number(s): B1AXR0, Q8C1S2, Q8CFU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 1, 2003
Last modified: September 7, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.